p53 domains: identification and characterization of two autonomous DNA-binding regions.

Abstract:

:We have investigated the DNA-binding, oligomerization, and trans-activation functions of isolated segments of murine p53. We find that p53 has two autonomous DNA-binding regions. One domain, from amino acid 280 to 390, forms stable tetramers and binds DNA nonspecifically. The biological significance, if any, of this DNA-binding activity is not known. A second domain, from amino acid 80 to 290, does not form stable tetramers under stringent conditions but binds DNA both specifically and nonspecifically. The specific DNA-binding function of p53, therefore, resides in the highly conserved central region of the protein and does not require stable tetramerization. Amino acids 1-290, which include both the specific DNA-binding domain and the amino-terminal acidic region, activate a p53-specific promoter in vivo. This finding strongly argues that the DNA-binding activity of p53 segment 80-290 is physiologically significant. The role of tetramerization in p53 function remains to be determined.

journal_name

Genes Dev

journal_title

Genes & development

authors

Wang Y,Reed M,Wang P,Stenger JE,Mayr G,Anderson ME,Schwedes JF,Tegtmeyer P

doi

10.1101/gad.7.12b.2575

subject

Has Abstract

pub_date

1993-12-01 00:00:00

pages

2575-86

issue

12B

eissn

0890-9369

issn

1549-5477

journal_volume

7

pub_type

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